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TRPM7 is essential for Mg2+ homeostasis in mammals

Author

Listed:
  • Lillia V. Ryazanova

    (University of Medicine and Dentistry of New Jersey/R. W. Johnson Medical School)

  • Lusliany J. Rondon

    (INRA, UMR 1019, UNH, CRNH Auvergne, and Clermont Université, Université d'Auvergne, Unité de Nutrition Humaine, BP 10448, Clermont-Ferrand F-63000, France.)

  • Susanna Zierler

    (Laboratory of Cell and Molecular Signaling, Queen's Center for Biomedical Research, The Queen's Medical Center and John A. Burns School of Medicine, University of Hawaii)

  • Zhixian Hu

    (University of Medicine and Dentistry of New Jersey/R. W. Johnson Medical School)

  • Joanna Galli

    (INRA, UMR 1019, UNH, CRNH Auvergne, and Clermont Université, Université d'Auvergne, Unité de Nutrition Humaine, BP 10448, Clermont-Ferrand F-63000, France.
    Faculty of Veterinary Medicine, Wroclaw University of Environmental and Life Sciences, Norwida 31, Wrocław 50-375, Poland.)

  • Terry P. Yamaguchi

    (Cancer and Developmental Biology Laboratory, Center for Cancer Research, National Cancer Institute-Frederick, NIH)

  • Andrzej Mazur

    (INRA, UMR 1019, UNH, CRNH Auvergne, and Clermont Université, Université d'Auvergne, Unité de Nutrition Humaine, BP 10448, Clermont-Ferrand F-63000, France.)

  • Andrea Fleig

    (Laboratory of Cell and Molecular Signaling, Queen's Center for Biomedical Research, The Queen's Medical Center and John A. Burns School of Medicine, University of Hawaii)

  • Alexey G. Ryazanov

    (University of Medicine and Dentistry of New Jersey/R. W. Johnson Medical School)

Abstract

Mg2+ is the second-most abundant cation in animal cells and is an essential cofactor in numerous enzymatic reactions. The molecular mechanisms controlling Mg2+ balance in the organism are not well understood. In this study, we report identification of TRPM7, a bifunctional protein containing a protein kinase fused to an ion channel, as a key regulator of whole body Mg2+ homeostasis in mammals. We generated TRPM7-deficient mice with the deletion of the kinase domain. Homozygous TRPM7Δkinase mice demonstrated early embryonic lethality, whereas heterozygous mice were viable, but developed signs of hypomagnesaemia and revealed a defect in intestinal Mg2+ absorption. Cells derived from heterozygous TRPM7Δkinase mice demonstrated reduced TRPM7 currents that had increased sensitivity to the inhibition by Mg2+. Embryonic stem cells lacking TRPM7 kinase domain displayed a proliferation arrest phenotype that can be rescued by Mg2+ supplementation. Our results demonstrate that TRPM7 is essential for the control of cellular and whole body Mg2+ homeostasis.

Suggested Citation

  • Lillia V. Ryazanova & Lusliany J. Rondon & Susanna Zierler & Zhixian Hu & Joanna Galli & Terry P. Yamaguchi & Andrzej Mazur & Andrea Fleig & Alexey G. Ryazanov, 2010. "TRPM7 is essential for Mg2+ homeostasis in mammals," Nature Communications, Nature, vol. 1(1), pages 1-9, December.
    • Handle: RePEc:nat:natcom:v:1:y:2010:i:1:d:10.1038_ncomms1108
    DOI: 10.1038/ncomms1108
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